Affiliations 

  • 1 Institut de la Nutrition, de l'Alimentation et des Technologies Agro-alimentaires INATAA 25017, Université Frères Mentouri, Constantine 1, Algeria
  • 2 Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 3 Department of Microbiology and Biotechnology, Federal University Dutse, Nigeria
Curr Res Food Sci, 2022;5:207-221.
PMID: 35106485 DOI: 10.1016/j.crfs.2022.01.011

Abstract

The inactivation of antinutritional factors, protease inhibitors within winged bean protein was induced by two respective method treatments. The physical method based on steam vapor that was conducted using an autoclave and chemical method consisting on pH-gradients of buffer solutions prepared at respective acidic pH, neutral pH and alkaline pH ranges. The activity of remaining protease inhibitors of bowman birk inhibitor (BBI), and kunitz-trypsin inhibitor (KTI) after and before treatments was enzymatically confirmed using relevant antagonistic trypsin and combined trypsin-α-chymotrypsin digests. The resulting molecular assembly indicating an interval molecular relaxation range of °0.16 < °DA < °0.2 corresponding to reconformation in protein units with volume-mass changes of -2.17 < ∂v' < +2.17 and with denaturation/unfolding efficiency based on heat capacity ΔCp of 36.36 < DE/UF% < 54.67. These structural changes had a great benefit in determining and producing functional protein hydrolysates.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.